ArticleJournal of bacteriology2009
An orthologue of Bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Longitudinal host-microbiome dynamics of metatranscription identify hallmarks of progression in periodontitis.Microbiome · 2025Article
- A bacterial sialidase mediates early-life colonization by a pioneering gut commensal.Cell host & microbe · 2024Article
- The Roles of Periodontal Bacteria in Atherosclerosis.International journal of molecular sciences · 2023Review
- Bacterial Sialic Acid Catabolism at the Host-Microbe Interface.Journal of microbiology (Seoul, Korea) · 2023Review
- The Association betweenInternational journal of environmental research and public health · 2022Article
- Article
- Sialylation and fucosylation modulate inflammasome-activating eIF2 Signaling and microbial translocation during HIV infection.Mucosal immunology · 2020Article
- Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia.BMC genomics · 2020Article
- Nonulosonic acids contribute to the pathogenicity of the oral bacteriumInterface focus · 2019Review
- Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacteriumThe Journal of biological chemistry · 2019Article
- Sialidases FromFrontiers in cellular and infection microbiology · 2019Review
- Sialic acid transporter NanT participates in Tannerella forsythia biofilm formation and survival on epithelial cells.Microbial pathogenesis · 2016Article
- Outer membrane vesicles of Tannerella forsythia: biogenesis, composition, and virulence.Molecular oral microbiology · 2015Article
- Sialic acid catabolism drives intestinal inflammation and microbial dysbiosis in mice.Nature communications · 2015Article
- Host Sialic Acids: A Delicacy for the Pathogen with Discerning Taste.Microbiology spectrum · 2015Review
- Chronic oral infection with major periodontal bacteria Tannerella forsythia modulates systemic atherosclerosis risk factors and inflammatory markers.Pathogens and disease · 2015Article
- Characterization of an α-l-fucosidase from the periodontal pathogen Tannerella forsythia.Virulence · 2015Article
- A surface-exposed neuraminidase affects complement resistance and virulence of the oral spirochaete Treponema denticola.Molecular microbiology · 2013Article
- Structure and immunogenicity of the rough-type lipopolysaccharide from the periodontal pathogen Tannerella forsythia.Clinical and vaccine immunology : CVI · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Sialidase activity is a putative virulence factor of the anaerobic periodontal pathogen Tannerella forsythia, but it is uncertain which genes encode this activity. Characterization of a putative sialidase, SiaHI, by others, indicated that this protein alone may not be responsible for all of the sialidase activity. We describe a second sialidase in T. forsythia (TF0035), an orthologue of Bacteroides fragilis NanH, and its expression in Escherichia coli. Sialidase activity of the expressed NanH was confirmed by using 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid as a substrate. Biochemical characterization of the recombinant T. forsythia NanH indicated that it was active over a broad pH range, with optimum activity at pH 5.5. This enzyme has high affinity for 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid (K(m) of 32.9 +/- 10.3 microM) and rapidly releases 4-methylumbelliferone (V(max) of 170.8 +/- 11.8 nmol of 4-methylumbelliferone min(-1) mg of protein(-1)). E. coli lysates containing recombinant T. forsythia NanH cleave sialic acid from a range of substrates, with a preference for alpha2-3 glycosidic linkages. The genes adjacent to nanH encode proteins apparently involved in the metabolism of sialic acid, indicating that the NanH sialidase is likely to be involved in nutrient acquisition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.